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Structural bioinformatics of enol pyruvyl shikimate phosphate synthase from Vibrio cholerae
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نویسنده
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iqbal a. ,azim m.k.
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منبع
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journal of the chemical society of pakistan - 2012 - دوره : 34 - شماره : 1 - صفحه:120 -126
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چکیده
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The enzymes of shikimate pathway are essential for fungi,algae,bacteria and plants and their absence in mammals have made these enzymes strong candidates for drug designing. the 5- enolpyruvylshikimate 3-phosphate synthase (epsp synthase) is the sixth enzyme of shikimate biosynthetic pathway. this agriculturally important enzyme is the prime target for the non-selective herbicide glyphosate. we have constructed tertiary structure of v. cholerae epsp synthase in open and closed conformations. protein structure prediction using homology modeling provided valuable information regarding structure function relationships of this enzyme. there are significant differences in the relative orientation of the two domains in open and closed conformations. the open conformation of epsp is prominent in the absence of substrate/inhibitor while it turns to closed conformation after binding to substrate/inhibitor which rotates the c-terminal domain at about 25 degrees.
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کلیدواژه
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Bioinformatics; EPSP synthase; Homology modeling; Vibrio cholerae
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آدرس
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international center for chemical and biological sciences,h.e.j. research institute of chemistry,university of karachi, Pakistan, international center for chemical and biological sciences,h.e.j. research institute of chemistry,university of karachi, Pakistan
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Authors
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